Sequence-based study of two related proteins with different folding behaviors

Summary, in English

Z(SPA-1) is an engineered protein that binds to its parent, the three-helix-bundle Z domain of staphylococcal protein A. Uncomplexed Z(SPA-1) shows a reduced helix content and a melting behavior that is less cooperative, compared with the wild-type Z domain. Here we show that the difference in folding behavior between these two sequences can be partly understood in terms of an off-lattice model with 5-6 atoms per amino acid and a minimalistic potential, in which folding is driven by backbone hydrogen bonding and effective hydrophobic attraction. (C) 2003 Wiley-Liss, Inc.

• Författare: Giorgio Favrin; Anders Irbäck; Stefan Wallin
• Avdelning/ar: Beräkningsbiologi och biologisk fysik - Genomgår omorganisation
• Publiceringsår: 2004
• Språk: Engelska
• Sidor: 8-12
• Publikation/Tidskrift/Serie: Proteins
• Volym: 54
• Issue: 1
• Länkar: http://dx.doi.org/10.1002/prot.10575
• Dokumenttyp: Artikel i tidskrift
• Förlag: John Wiley & Sons Inc.
• Ämne: Biophysics
• Nyckelord: bundle; Monte Carlo simulation; folding thermodynamics; protein folding; folding kinetics; three-helix; unstructured protein
• Status: Published
• ISBN/ISSN/Övrigt: ISSN: 0887-3585